Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform)

 DCE2_HUMAN              Reviewed;         585 AA.
Q05329; Q9UD87;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
23-MAY-2018, entry version 156.
RecName: Full=Glutamate decarboxylase 2;
EC=4.1.1.15;
AltName: Full=65 kDa glutamic acid decarboxylase;
Short=GAD-65;
AltName: Full=Glutamate decarboxylase 65 kDa isoform;
Name=GAD2; Synonyms=GAD65;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreatic islet;
PubMed=1924293; DOI=10.1073/pnas.88.19.8337;
Karlsen A.E., Hagopian W.A., Grubin C.E., Dube S., Disteche C.M.,
Adler D.A., Barmeier H., Mathewes S., Grant F.J., Foster D.,
Lernmark A.;
"Cloning and primary structure of a human islet isoform of glutamic
acid decarboxylase from chromosome 10.";
Proc. Natl. Acad. Sci. U.S.A. 88:8337-8341(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1549570; DOI=10.1073/pnas.89.6.2115;
Bu D.-F., Erlander M.G., Hitz B.C., Tillakaratne N.J., Kaufman D.L.,
Wagner-Mcpherson C.B., Evans G.A., Tobin A.J.;
"Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are
each encoded by a single gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:2115-2119(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8088791; DOI=10.1006/geno.1994.1246;
Bu D.-F., Tobin A.J.;
"The exon-intron organization of the genes (GAD1 and GAD2) encoding
two human glutamate decarboxylases (GAD67 and GAD65) suggests that
they derive from a common ancestral GAD.";
Genomics 21:222-228(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-12; ASN-124;
ARG-286 AND GLN-375.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-585.
TISSUE=Pancreas;
PubMed=7680313; DOI=10.1111/j.1432-1033.1993.tb17698.x;
Mauch L., Abney C.C., Berg H., Scherbaum W.A., Liedvogel B.,
Northemann W.;
"Characterization of a linear epitope within the human pancreatic 64-
kDa glutamic acid decarboxylase and its autoimmune recognition by sera
from insulin-dependent diabetes mellitus patients.";
Eur. J. Biochem. 212:597-603(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 245-585.
PubMed=8243826; DOI=10.2337/diab.42.12.1799;
Kim J., Richter W., Aanstoot H.-J., Shi Y., Fu Q., Rajotte R.,
Warnock G., Baekkeskov S.;
"Differential expression of GAD65 and GAD67 in human, rat, and mouse
pancreatic islets.";
Diabetes 42:1799-1808(1993).
[7]
PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8999827; DOI=10.1074/jbc.272.3.1548;
Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.;
"Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes
membrane anchored from soluble glutamic acid decarboxylase 65 and is
restricted to glutamic acid decarboxylase 65alpha.";
J. Biol. Chem. 272:1548-1557(1997).
[8]
SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-30 AND CYS-45.
PubMed=12356867; DOI=10.1083/jcb.200205053;
Kanaani J., El-Din El-Husseini A., Aguilera-Moreno A., Diacovo J.M.,
Bredt D.S., Baekkeskov S.;
"A combination of three distinct trafficking signals mediates axonal
targeting and presynaptic clustering of GAD65.";
J. Cell Biol. 158:1229-1238(2002).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 222-235 IN COMPLEX WITH MHC.
PubMed=10775108; DOI=10.1126/science.288.5465.505;
Corper A.L., Stratmann T., Apostolopoulos V., Scott C.A., Garcia K.C.,
Kang A.S., Wilson I.A., Teyton L.;
"A structural framework for deciphering the link between I-Ag7 and
autoimmune diabetes.";
Science 288:505-511(2000).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-584 IN COMPLEX WITH
SUBSTRATE, SUBUNIT, AND COFACTOR.
PubMed=17384644; DOI=10.1038/nsmb1228;
Fenalti G., Law R.H.P., Buckle A.M., Langendorf C., Tuck K.,
Rosado C.J., Faux N.G., Mahmood K., Hampe C.S., Banga J.P., Wilce M.,
Schmidberger J., Rossjohn J., El-Kabbani O., Pike R.N., Smith A.I.,
Mackay I.R., Rowley M.J., Whisstock J.C.;
"GABA production by glutamic acid decarboxylase is regulated by a
dynamic catalytic loop.";
Nat. Struct. Mol. Biol. 14:280-286(2007).
-!- FUNCTION: Catalyzes the production of GABA.
-!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:17384644};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.15 mM for glutamate {ECO:0000269|PubMed:8999827};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10775108,
ECO:0000269|PubMed:17384644}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-9304251, EBI-741181;
Q15041:ARL6IP1; NbExp=5; IntAct=EBI-9304251, EBI-714543;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-9304251, EBI-2548702;
Q969L2:MAL2; NbExp=5; IntAct=EBI-9304251, EBI-944295;
Q96B96:TMEM159; NbExp=5; IntAct=EBI-9304251, EBI-7055862;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12356867}. Cytoplasmic vesicle
{ECO:0000269|PubMed:12356867}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:12356867}; Lipid-anchor
{ECO:0000269|PubMed:12356867}. Golgi apparatus membrane
{ECO:0000269|PubMed:12356867}; Peripheral membrane protein
{ECO:0000269|PubMed:12356867}; Cytoplasmic side
{ECO:0000269|PubMed:12356867}. Note=Associated to cytoplasmic
vesicles. In neurons, cytosolic leaflet of Golgi membranes and
presynaptic clusters.
-!- PTM: Phosphorylated; which does not affect kinetic parameters or
subcellular location. {ECO:0000269|PubMed:8999827}.
-!- PTM: Palmitoylated; which is required for presynaptic clustering.
{ECO:0000269|PubMed:12356867}.
-!- SIMILARITY: Belongs to the group II decarboxylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA49554.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gad2/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M81882; AAA62367.1; -; mRNA.
EMBL; M74826; AAA58491.1; -; mRNA.
EMBL; AY340073; AAP88040.1; -; Genomic_DNA.
EMBL; X69936; CAA49554.1; ALT_INIT; mRNA.
EMBL; M70435; AAA52513.1; -; mRNA.
CCDS; CCDS7149.1; -.
PIR; A41935; A41292.
RefSeq; NP_000809.1; NM_000818.2.
RefSeq; NP_001127838.1; NM_001134366.1.
UniGene; Hs.231829; -.
PDB; 1ES0; X-ray; 2.60 A; B=207-220.
PDB; 2OKK; X-ray; 2.30 A; A=88-584.
PDBsum; 1ES0; -.
PDBsum; 2OKK; -.
ProteinModelPortal; Q05329; -.
SMR; Q05329; -.
BioGrid; 108846; 8.
DIP; DIP-29293N; -.
IntAct; Q05329; 19.
STRING; 9606.ENSP00000259271; -.
ChEMBL; CHEMBL2952; -.
DrugBank; DB00142; L-Glutamic Acid.
iPTMnet; Q05329; -.
PhosphoSitePlus; Q05329; -.
SwissPalm; Q05329; -.
BioMuta; GAD2; -.
DMDM; 1352216; -.
PaxDb; Q05329; -.
PeptideAtlas; Q05329; -.
PRIDE; Q05329; -.
DNASU; 2572; -.
Ensembl; ENST00000259271; ENSP00000259271; ENSG00000136750.
Ensembl; ENST00000376261; ENSP00000365437; ENSG00000136750.
GeneID; 2572; -.
KEGG; hsa:2572; -.
CTD; 2572; -.
DisGeNET; 2572; -.
EuPathDB; HostDB:ENSG00000136750.11; -.
GeneCards; GAD2; -.
HGNC; HGNC:4093; GAD2.
HPA; CAB078177; -.
HPA; HPA044637; -.
MIM; 138275; gene.
neXtProt; NX_Q05329; -.
OpenTargets; ENSG00000136750; -.
PharmGKB; PA28508; -.
eggNOG; KOG0629; Eukaryota.
eggNOG; COG0076; LUCA.
GeneTree; ENSGT00760000119205; -.
HOGENOM; HOG000005382; -.
HOVERGEN; HBG004980; -.
InParanoid; Q05329; -.
KO; K01580; -.
OMA; WRAKGTT; -.
OrthoDB; EOG091G07ZU; -.
PhylomeDB; Q05329; -.
TreeFam; TF314688; -.
BioCyc; MetaCyc:HS06208-MONOMER; -.
BRENDA; 4.1.1.15; 2681.
Reactome; R-HSA-888568; GABA synthesis.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
SABIO-RK; Q05329; -.
EvolutionaryTrace; Q05329; -.
GeneWiki; GAD2; -.
GenomeRNAi; 2572; -.
PRO; PR:Q05329; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000136750; -.
CleanEx; HS_GAD2; -.
ExpressionAtlas; Q05329; baseline and differential.
Genevisible; Q05329; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
GO; GO:0004351; F:glutamate decarboxylase activity; TAS:Reactome.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0006540; P:glutamate decarboxylation to succinate; TAS:ProtInc.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
Gene3D; 3.40.640.10; -; 1.
InterPro; IPR002129; PyrdxlP-dep_de-COase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
InterPro; IPR021115; Pyridoxal-P_BS.
Pfam; PF00282; Pyridoxal_deC; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Decarboxylase; Golgi apparatus;
Lipoprotein; Lyase; Membrane; Neurotransmitter biosynthesis;
Palmitate; Phosphoprotein; Polymorphism; Pyridoxal phosphate;
Reference proteome; Synapse.
CHAIN 1 585 Glutamate decarboxylase 2.
/FTId=PRO_0000146968.
REGION 181 183 Substrate binding.
BINDING 558 558 Substrate. {ECO:0000269|PubMed:17384644}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000269|PubMed:8999827}.
MOD_RES 396 396 N6-(pyridoxal phosphate)lysine.
LIPID 30 30 S-palmitoyl cysteine.
{ECO:0000269|PubMed:12356867}.
LIPID 45 45 S-palmitoyl cysteine.
{ECO:0000269|PubMed:12356867}.
VARIANT 12 12 G -> R (in dbSNP:rs8190591).
{ECO:0000269|Ref.4}.
/FTId=VAR_018821.
VARIANT 124 124 K -> N (in dbSNP:rs8190600).
{ECO:0000269|Ref.4}.
/FTId=VAR_018822.
VARIANT 153 153 P -> Q (in dbSNP:rs2839672).
/FTId=VAR_029176.
VARIANT 232 232 G -> E (in dbSNP:rs2839673).
/FTId=VAR_029177.
VARIANT 286 286 K -> R (in dbSNP:rs8190671).
{ECO:0000269|Ref.4}.
/FTId=VAR_018823.
VARIANT 326 326 G -> A (in dbSNP:rs2839678).
/FTId=VAR_029178.
VARIANT 375 375 R -> Q (in dbSNP:rs8190730).
{ECO:0000269|Ref.4}.
/FTId=VAR_018824.
HELIX 89 91 {ECO:0000244|PDB:2OKK}.
HELIX 94 96 {ECO:0000244|PDB:2OKK}.
HELIX 104 126 {ECO:0000244|PDB:2OKK}.
HELIX 138 144 {ECO:0000244|PDB:2OKK}.
HELIX 156 169 {ECO:0000244|PDB:2OKK}.
STRAND 178 183 {ECO:0000244|PDB:2OKK}.
HELIX 188 200 {ECO:0000244|PDB:2OKK}.
TURN 207 209 {ECO:0000244|PDB:2OKK}.
HELIX 211 228 {ECO:0000244|PDB:2OKK}.
HELIX 231 233 {ECO:0000244|PDB:2OKK}.
STRAND 235 242 {ECO:0000244|PDB:2OKK}.
HELIX 243 258 {ECO:0000244|PDB:2OKK}.
HELIX 262 265 {ECO:0000244|PDB:2OKK}.
HELIX 267 269 {ECO:0000244|PDB:2OKK}.
STRAND 273 278 {ECO:0000244|PDB:2OKK}.
HELIX 284 291 {ECO:0000244|PDB:2OKK}.
HELIX 296 298 {ECO:0000244|PDB:2OKK}.
STRAND 299 302 {ECO:0000244|PDB:2OKK}.
HELIX 312 324 {ECO:0000244|PDB:2OKK}.
STRAND 328 337 {ECO:0000244|PDB:2OKK}.
TURN 339 341 {ECO:0000244|PDB:2OKK}.
HELIX 347 357 {ECO:0000244|PDB:2OKK}.
STRAND 360 365 {ECO:0000244|PDB:2OKK}.
HELIX 368 373 {ECO:0000244|PDB:2OKK}.
TURN 375 377 {ECO:0000244|PDB:2OKK}.
HELIX 378 381 {ECO:0000244|PDB:2OKK}.
HELIX 384 386 {ECO:0000244|PDB:2OKK}.
STRAND 388 392 {ECO:0000244|PDB:2OKK}.
STRAND 405 411 {ECO:0000244|PDB:2OKK}.
HELIX 414 419 {ECO:0000244|PDB:2OKK}.
HELIX 435 437 {ECO:0000244|PDB:2OKK}.
HELIX 440 442 {ECO:0000244|PDB:2OKK}.
HELIX 452 486 {ECO:0000244|PDB:2OKK}.
STRAND 491 497 {ECO:0000244|PDB:2OKK}.
STRAND 500 502 {ECO:0000244|PDB:2OKK}.
STRAND 504 508 {ECO:0000244|PDB:2OKK}.
TURN 511 515 {ECO:0000244|PDB:2OKK}.
HELIX 523 526 {ECO:0000244|PDB:2OKK}.
HELIX 529 540 {ECO:0000244|PDB:2OKK}.
STRAND 544 550 {ECO:0000244|PDB:2OKK}.
STRAND 553 559 {ECO:0000244|PDB:2OKK}.
HELIX 568 581 {ECO:0000244|PDB:2OKK}.
SEQUENCE 585 AA; 65411 MW; 0322509F0E2C32EE CRC64;
MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
PGGAISNMYA MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQNCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH VDKCLELAEY
LYNIIKNREG YEMVFDGKPQ HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL


Related products :

Catalog number Product name Quantity
18-783-77681 RABBIT ANTI HUMAN GLUTAMATE DECARBOXYLASE - GLUTAMATE DEHYDROGENASE; EC 4.1.1.15; Glutamate decarboxylase 67 kDa isoform; GAD-67; 67 kDa glutamic acid decarboxylase Polyclonal 0.05 ml
U1258h CLIA 67 kDa glutamic acid decarboxylase,GAD,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Homo sapiens,Human 96T
E1258h ELISA kit 67 kDa glutamic acid decarboxylase,GAD,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Homo sapiens,Human 96T
E1258h ELISA 67 kDa glutamic acid decarboxylase,GAD,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Homo sapiens,Human 96T
E1258m ELISA 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Mouse,Mus musculus 96T
E1258r ELISA 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Rat,Rattus norvegicus 96T
U1258r CLIA 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Rat,Rattus norvegicus 96T
E1258r ELISA kit 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Rat,Rattus norvegicus 96T
U1258m CLIA 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Mouse,Mus musculus 96T
EIAAB10595 65 kDa glutamic acid decarboxylase,GAD2,GAD65,GAD-65,Glutamate decarboxylase 2,Glutamate decarboxylase 65 kDa isoform,Homo sapiens,Human
E1258m ELISA kit 67 kDa glutamic acid decarboxylase,Gad1,Gad67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Mouse,Mus musculus 96T
E1258p ELISA kit 67 kDa glutamic acid decarboxylase,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Pig,Sus scrofa 96T
E1258p ELISA 67 kDa glutamic acid decarboxylase,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Pig,Sus scrofa 96T
18-783-77682 RABBIT ANTI HUMAN GAD 65 - GLUTAMATE DECARBOXYLASE; EC 4.1.1.15; Glutamate decarboxylase 67 kDa isoform; GAD-67; 67 kDa glutamic acid decarboxylase Polyclonal 1 ml
EIAAB10594 65 kDa glutamic acid decarboxylase,Gad2,Gad65,GAD-65,Glutamate decarboxylase 2,Glutamate decarboxylase 65 kDa isoform,Mouse,Mus musculus
U1258p CLIA 67 kDa glutamic acid decarboxylase,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform,Pig,Sus scrofa 96T
EIAAB10592 65 kDa glutamic acid decarboxylase,Gad2,Gad65,GAD-65,Glutamate decarboxylase 2,Glutamate decarboxylase 65 kDa isoform,Rat,Rattus norvegicus
EIAAB10591 65 kDa glutamic acid decarboxylase,GAD2,GAD65,GAD-65,Glutamate decarboxylase 2,Glutamate decarboxylase 65 kDa isoform,Pig,Sus scrofa
E1258c ELISA kit 67 kDa glutamic acid decarboxylase,Canis familiaris,Canis lupus familiaris,Dog,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform 96T
E1258c ELISA 67 kDa glutamic acid decarboxylase,Canis familiaris,Canis lupus familiaris,Dog,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform 96T
U1258c CLIA 67 kDa glutamic acid decarboxylase,Canis familiaris,Canis lupus familiaris,Dog,GAD1,GAD67,GAD-67,Glutamate decarboxylase 1,Glutamate decarboxylase 67 kDa isoform 96T
EIAAB10593 65 kDa glutamic acid decarboxylase,Canis familiaris,Canis lupus familiaris,Dog,GAD2,GAD65,GAD-65,Glutamate decarboxylase 2,Glutamate decarboxylase 65 kDa isoform
18-783-77683 RABBIT ANTI HUMAN GLUTAMATE DECARBOXYLASE 65kDa ISOFORM - GLUTAMATE DECARBOXYLASE; Polyclonal 1 ml
18-783-77684 RABBIT ANTI HUMAN GLUTAMATE DECARBOXYLASE 67kDa ISOFORM - GLUTAMATE DECARBOXYLASE Polyclonal 1 ml
18-272-196353 GAD65 prediluted - Rabbit polyclonal to GAD65 prediluted; EC 4.1.1.15; Glutamate decarboxylase 65 kDa isoform; GAD-65; 65 kDa glutamic acid decarboxylase Polyclonal 7 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur